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Fig. 3 Coumestrol inhibits the activity of DYRK1A by occupying its ATP-binding site. Schematic showing x-ray crystallography of the interaction between DYRK1A and coumestrol, with coumestrol occupying the ATP-binding site of DYRK1A.
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Reprinted from International journal of biological macromolecules, 282(Pt 4), Peng, C.H., Hwang, T.L., Hung, S.C., Tu, H.J., Tseng, Y.T., Lin, T.E., Lee, C.C., Tseng, Y.C., Ko, C.Y., Yen, S.C., Hsu, K.C., Pan, S.L., HuangFu, W.C., Identification, biological evaluation, and crystallographic analysis of coumestrol as a novel dual-specificity tyrosine-phosphorylation-regulated kinase 1A inhibitor, 136860, Copyright (2024) with permission from Elsevier. Full text @ Int. J. Biol. Macromol.